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New insights into processing of bovine viral diarrhea virus glycoproteins E^rns and E1

Institute of Diagnostic Virology, Friedrich-Loeffler-Institut, Suedufer 10, 17493 Greifswald-Insel Riems, Germany

Correspondence
Martin Beer
martin.beer{at}fli.bund.de

Bovine viral diarrhea virus (BVDV) is a member of the genus Pestivirus within the family Flaviviridae. Its single-stranded RNA encodes a polyprotein that is cleaved co- and post-translationally by viral and cellular proteases. However, the cleavage between the envelope proteins E^rns and E1 is still unexplained. In this study, an E^rns–E1 protein could be identified and characterized with a new E1-specific antiserum. With bicistronic constructs bearing a deletion in the E^rns-encoding region and expressing E^rns or the E^rns–E1 protein, it could be shown that this protein is not essential for virus replication. Furthermore, two putative cleavage sites were mutated in eukaryotic expression plasmids, as well as in full-length cDNA constructs. The mutation of position P3 of a potential signal peptide peptidase site abolished cleavage completely and no infectious virus progeny could be observed, indicating that cleavage of the E^rns–E1 protein is indispensable for virus growth.